4RIQ

Crystal structure of DPY-30 dimerization/docking domain in complex with Ash2L Sdc1-DPY-30 Interacting region (SDI)

Summary for 4RIQ

• Entry DOI: 10.2210/pdb4riq/pdb
• Descriptor: Protein dpy-30 homolog, Set1/Ash2 histone methyltransferase complex subunit ASH2, SULFATE ION, ... (4 entities in total)
• Functional Keywords: histone, chromatin, methylation, dimerization/docking module, allosteric regulator, ash2l, wdr5, rbbp5, mll1, mll2, mll3, mll4, set1a, set1b, transferase-protein binding complex, transferase/protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : Q9C005 Q9UBL3
• Total number of polymer chains: 24
• Total formula weight: 126007.79

Authors

Tremblay, V.,Couture, J.-F. (deposition date: 2014-10-07, release date: 2014-12-17, Last modification date: 2024-02-28)

Primary citation

Tremblay, V.,Zhang, P.,Chaturvedi, C.P.,Thornton, J.,Brunzelle, J.S.,Skiniotis, G.,Shilatifard, A.,Brand, M.,Couture, J.F.
Molecular Basis for DPY-30 Association to COMPASS-like and NURF Complexes.
Structure, 22:1821-1830, 2014

PubMed Abstract: DPY-30 is a subunit of mammalian COMPASS-like complexes (complex of proteins associated with Set1) and regulates global histone H3 Lys-4 trimethylation. Here we report structural evidence showing that the incorporation of DPY-30 into COMPASS-like complexes is mediated by several hydrophobic interactions between an amphipathic α helix located on the C terminus of COMPASS subunit ASH2L and the inner surface of the DPY-30 dimerization/docking (D/D) module. Mutations impairing the interaction between ASH2L and DPY-30 result in a loss of histone H3K4me3 at the β locus control region and cause a delay in erythroid cell terminal differentiation. Using overlay assays, we defined a consensus sequence for DPY-30 binding proteins and found that DPY-30 interacts with BAP18, a subunit of the nucleosome remodeling factor complex. Overall, our results indicate that the ASH2L/DPY-30 complex is important for cell differentiation and provide insights into the ability of DPY-30 to associate with functionally divergent multisubunit complexes.

PubMed: 25456412
DOI: 10.1016/j.str.2014.10.002

Experimental method

X-RAY DIFFRACTION (2.231 Å)